What functions do linker histones provide?
- 28 June 2004
- journal article
- review article
- Published by Wiley in Molecular Microbiology
- Vol. 53 (3) , 771-775
- https://doi.org/10.1111/j.1365-2958.2004.04195.x
Abstract
Linker histones have long been known to facilitate chromatin condensation in vitro. For many years, this activity led to speculation that these proteins function as global repressors of transcription. However, work from numerous systems has demonstrated that this is not the case, and that linker histones appear to affect only the transcription of a small subset of genes, and, in fact, act to activate as well as repress transcription. Furthermore, there is evidence that suggests that linker histones are not required for mitotic condensation. In this review, we focus on studies of biological functions of linker histones primarily performed in unicellular eukaryotes. We highlight recent developments pointing towards linker histone involvement in DNA repair and ageing, which raise the possibility that the biological functions of linker histones are more varied than previously imagined.Keywords
This publication has 35 references indexed in Scilit:
- Two Homologous Domains of Similar Structure but Different Stability in the Yeast Linker Histone, Hho1pJournal of Molecular Biology, 2004
- Distinct Properties of the Two Putative “Globular Domains” of the Yeast Linker Histone, Hho1pJournal of Molecular Biology, 2004
- H1 Linker Histones Are Essential for Mouse Development and Affect Nucleosome Spacing In VivoMolecular and Cellular Biology, 2003
- Rad54 protein possesses chromatin-remodeling activity stimulated by the Rad51–ssDNA nucleoprotein filamentNature Structural & Molecular Biology, 2003
- Are linker histones (histone H1) dispensable for survival?BioEssays, 2000
- Winged helix proteinsCurrent Opinion in Structural Biology, 2000
- Eukaryotic-like histones in ChlamydiaFrontiers in Bioscience-Landmark, 1998
- Where is the globular domain of linker histone located on the nucleosome?Trends in Biochemical Sciences, 1997
- DNA binding of the Bordetella pertussis H1 homolog alters in vitro DNA flexibilityJournal of Bacteriology, 1996
- Homo- and Heteronuclear Two-Dimensional NMR Studies of the Globular Domain of Histone H1: Full Assignment, Tertiary Structure, and Comparison with the Globular Domain of Histone H5Biochemistry, 1994